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<jats:p>The extent of terrestrial vertebrate extinctions at the end of the Cretaceous is poorly understood, and estimates have ranged from a mass extinction to limited extinctions of specific groups. Molecular and paleontological data demonstrate that modern bird orders started diverging in the Early Cretaceous; at least 22 avian lineages of modern birds cross the Cretaceous-Tertiary boundary. Data for several other terrestrial vertebrate groups indicate a similar pattern of survival and, taken together, favor incremental changes during a Cretaceous diversification of birds and mammals rather than an explosive radiation in the Early Tertiary.</jats:p>

<jats:p>During running, muscles and tendons must absorb and release mechanical work to maintain the cyclic movements of the body and limbs, while also providing enough force to support the weight of the body. Direct measurements of force and fiber length in the lateral gastrocnemius muscle of running turkeys revealed that the stretch and recoil of tendon and muscle springs supply mechanical work while active muscle fibers produce high forces. During level running, the active muscle shortens little and performs little work but provides the force necessary to support body weight economically. Running economy is improved by muscles that act as active struts rather than working machines.</jats:p>

<jats:p>Predawn episodes of mass spawning by green algae (up to nine species in five genera on a single morning) intermittently cloud Caribbean waters. Species- and sex-specific bouts of anisogamous gamete release occurred synchronously and predictably on a given morning, with closely related species spawning at different times. Algal sexual reproduction was seasonal, but, unlike the mass-spawning behavior of other sessile marine organisms, showed no lunar or tidal cycling. The discovery of mass-spawning behavior by these algae has important implications for future studies of the reproductive ecology and speciation of a vital, yet poorly understood, component of the coral reef community.</jats:p>

<jats:p> Phototransduction in <jats:italic>Drosophila</jats:italic> occurs through the ubiquitous phosphoinositide-mediated signal transduction system. Major unresolved questions in this pathway are the identity and role of the internal calcium stores in light excitation and the mechanism underlying regulation of Ca <jats:sup>2+</jats:sup> release from internal stores. Treatment of <jats:italic>Drosophila</jats:italic> photoreceptors with ryanodine and caffeine disrupted the current induced by light, whereas subsequent application of calcium-calmodulin (Ca-CaM) rescued the inactivated photoresponse. In calcium-deprived wild-type <jats:italic>Drosophila</jats:italic> and in calmodulin-deficient transgenic flies, the current induced by light was disrupted by a specific inhibitor of Ca-CaM. Furthermore, inhibition of Ca-CaM revealed light-induced release of calcium from intracellular stores. It appears that functional ryanodine-sensitive stores are essential for the photoresponse. Moreover, calcium release from these stores appears to be a component of <jats:italic>Drosophila</jats:italic> phototransduction, and Ca-CaM regulates this process. </jats:p>

<jats:p> Previous genetic studies of the nematode <jats:italic>Caenorhabditis elegans</jats:italic> identified three important components of the cell death machinery. CED-3 and CED-4 function to kill cells, whereas CED-9 protects cells from death. Here CED-9 and its mammalian homolog Bcl-x <jats:sub>L</jats:sub> (a member of the Bcl-2 family of cell death regulators) were both found to interact with and inhibit the function of CED-4. In addition, analysis revealed that CED-4 can simultaneously interact with CED-3 and its mammalian counterparts interleukin-1β-converting enzyme (ICE) and FLICE. Thus, CED-4 plays a central role in the cell death pathway, biochemically linking CED-9 and the Bcl-2 family to CED-3 and the ICE family of pro-apoptotic cysteine proteases. </jats:p>

<jats:p> The <jats:italic>Caenorhabditis elegans</jats:italic> survival gene <jats:italic>ced-9</jats:italic> regulates <jats:italic>ced-4</jats:italic> activity and inhibits cell death, but the mechanism by which this occurs is unknown. Through a genetic screen for CED-4-binding proteins, CED-9 was identified as an interacting partner of CED-4. CED-9, but not loss-of-function mutants, associated specifically with CED-4 in yeast or mammalian cells. The CED-9 protein localized primarily to intracellular membranes and the perinuclear region, whereas CED-4 was distributed in the cytosol. Expression of CED-9, but not a mutant lacking the carboxy-terminal hydrophobic domain, targeted CED-4 from the cytosol to intracellular membranes in mammalian cells. Thus, the actions of CED-4 and CED-9 are directly linked, which could provide the basis for the regulation of programmed cell death in <jats:italic>C. elegans.</jats:italic> </jats:p>

<jats:p>Bcl-2 is an integral membrane protein located mainly on the outer membrane of mitochondria. Overexpression of Bcl-2 prevents cells from undergoing apoptosis in response to a variety of stimuli. Cytosolic cytochrome c is necessary for the initiation of the apoptotic program, suggesting a possible connection between Bcl-2 and cytochrome c, which is normally located in the mitochondrial intermembrane space. Cells undergoing apoptosis were found to have an elevation of cytochrome c in the cytosol and a corresponding decrease in the mitochondria. Overexpression of Bcl-2 prevented the efflux of cytochrome c from the mitochondria and the initiation of apoptosis. Thus, one possible role of Bcl-2 in prevention of apoptosis is to block cytochrome c release from mitochondria.</jats:p>

<jats:p>In a cell-free apoptosis system, mitochondria spontaneously released cytochrome c, which activated DEVD-specific caspases, leading to fodrin cleavage and apoptotic nuclear morphology. Bcl-2 acted in situ on mitochondria to prevent the release of cytochrome c and thus caspase activation. During apoptosis in intact cells, cytochrome c translocation was similarly blocked by Bcl-2 but not by a caspase inhibitor, zVAD-fmk. In vitro, exogenous cytochrome c bypassed the inhibitory effect of Bcl-2. Cytochrome c release was unaccompanied by changes in mitochondrial membrane potential. Thus, Bcl-2 acts to inhibit cytochrome c translocation, thereby blocking caspase activation and the apoptotic process.</jats:p>

<jats:p> Basal transcription from the human RNA polymerase III U6 promoter depends on a TATA box that recruits the TATA box-binding protein (TBP) and a proximal sequence element that recruits the small nuclear RNA (snRNA)-activating protein complex (SNAP <jats:sub>c</jats:sub> ). TBP consists of a conserved carboxyl-terminal domain that performs all known functions of the protein and a nonconserved amino-terminal region of unknown function. Here, the amino-terminal region is shown to down-regulate binding of TBP to the U6 TATA box, mediate cooperative binding with SNAP <jats:sub>c</jats:sub> to the U6 promoter, and enhance U6 transcription. </jats:p>

<jats:p>The x-ray structures of three esterase-like catalytic antibodies identified by screening for catalytic activity the entire hybridoma repertoire, elicited in response to a phosphonate transition state analog (TSA) hapten, were analyzed. The high resolution structures account for catalysis by transition state stabilization, and in all three antibodies a tyrosine residue participates in the oxyanion hole. Despite significant conformational differences in their combining sites, the three antibodies, which are the most efficient among those elicited, achieve catalysis in essentially the same mode, suggesting that evolution for binding to a single TSA followed by screening for catalysis lead to antibodies with structural convergence.</jats:p>